ArticleFrontiers in microbiology2025
Recombinant expression and immunogenicity verification of Dabie bandavirus proteins Gn and Gc.
Article in Frontiers in microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Genotype-Specific Amino Acid Signatures in the Gn/Gc Glycoprotein of Severe Fever with Thrombocytopenia Syndrome Virus Associated with Neurological Symptoms.Pathogens (Basel, Switzerland) · 2026Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Introduction: Dabie bandavirus (DBV), a newly identified pathogen transmitted to humans via ticks bites, is the etiologic agent of severe fever with thrombocytopenia syndrome (SFTS). This disease is associated with a high mortality rate and constitutes a substantial threat to global public health. This study aimed to recombinantly express and characterize the immunogenicity and antigenicity of the DBV envelope proteins Gn and Gc. Methods: The recombinant plasmids pET15b-Gn and pET15b-Gc were constructed and expressed in Results: The rGn and rGc proteins were successfully expressed and purified, exhibiting molecular weights consistent with theoretical predictions. Antibody titers in immunized rabbits reached 1:512,000 for anti-rGn-IgG and 1:256,000 for anti-rGc-IgG. The proteins showed no significant cross-reactivity with other prevalent arboviruses. When used as antigens in assays, the rGn- and rGc-coated plates detected DBV IgM antibodies in 84.21% and 89.47% of positive samples, respectively. Discussion: This study confirmed that the prokaryotically expressed DBV Gn and Gc proteins possess favorable immunogenicity, addressing the critical knowledge gap in evaluating of the immunogenic efficacy of prokaryotically expressed Gn and Gc. Currently, research on DBV's pathogenic mechanisms, protein structure, and functions remains limited, and this findings provide a foundation for the development of DBV-related vaccines and drugs.
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